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Reviewed, UniProtKB/Swiss-Prot P16615 (AT2A2_HUMAN)

Last modified February 9, 2010. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
      Short name=SR Ca(2+)-ATPase 2
      Short name=SERCA2
    EC=3.6.3.8
Alternative name(s):
    Calcium pump 2
    Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
    Endoplasmic reticulum class 1/2 Ca(2+) ATPase
Gene names
Name: ATP2A2
Synonyms: ATP2B
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1042 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform SERCA2A is involved in the regulation of the contraction/relaxation cycle.

Catalytic activity

ATP + H2O + Ca2+(Cis) = ADP + phosphate + Ca2+(Trans).

Enzyme regulation

Reversibly inhibited by phospholamban (PLN) at low calcium concentrations. Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium. This inhibition is regulated by the phosphorylation of PLN By similarity.

Subunit structure

Associated with phospholamban (PLN) By similarity. Isoform SERCA2B interacts with TRAM2 (via C-terminus). Interacts with HAX1. Ref.3 Ref.10

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein.

Tissue specificity

Isoform SERCA2A is highly expressed in heart and slow twitch skeletal muscle. Isoform SERCA2B is widely expressed, in smooth muscle and nonmuscle tissues such as in adult skin epidermis. Ref.14

Post-translational modification

Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity.

Involvement in disease

Defects in ATP2A2 are a cause of acrokeratosis verruciformis (AKV) [MIM:101900]; also known as Hopf disease. AKV is a localized disorder of keratinization, which is inherited as an autosomal dominant trait. Its onset is early in life with multiple flat-topped, flesh-colored papules on the hands and feet, punctate keratoses on the palms and soles, with varying degrees of nail involvement. The histopathology shows a distinctive pattern of epidermal features with hyperkeratosis, hypergranulosis, and acanthosis together with papillomatosis. These changes are frequently associated with circumscribed elevations of the epidermis that are said to resemble church spires. There are no features of dyskeratosis or acantholysis, the typical findings in lesions of Darier disease. Ref.17

Defects in ATP2A2 are the cause of Darier disease (DD) [MIM:124200]; also known as Darier-White disease (DAR). DD is an autosomal dominantly inherited skin disorder characterized by loss of adhesion between epidermal cells (acantholysis) and abnormal keratinization. Patients with mild disease may have no more than a few scattered keratotic papules or subtle nail changes, whereas those with severe disease are handicapped by widespread malodorous keratotic plaques. In a few families, neuropsychiatric abnormalities such as mild mental retardation, schizophrenia, bipolar disorder and epilepsy have been reported. Stress, UV exposure, heat, sweat, friction, and oral contraception exacerbate disease symptoms. Prevalence has been estimated at 1 in 50000. Ref.14 Ref.13 Ref.15 Ref.16

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. Type IIA subfamily.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Epilepsy
   DomainTransmembrane
   LigandATP-binding
Calcium
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
Isopeptide bond
Nitration
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

cell adhesion Ref.16

Traceable author statement. Source: ProtInc

epidermis development Ref.16

Traceable author statement. Source: ProtInc

sarcoplasmic reticulum calcium ion transport

Traceable author statement. Source: UniProtKB

   Cellular componentintegral to plasma membrane Ref.1

Traceable author statement. Source: ProtInc

microsome Ref.1

Traceable author statement. Source: ProtInc

sarcoplasmic reticulum membrane

Traceable author statement. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

S100 alpha binding

Inferred from physical interaction. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-transporting ATPase activity Ref.1

Traceable author statement. Source: ProtInc

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PTP4A3O753651EBI-358933,EBI-1043866

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: SERCA2 transcripts differ only in their 3'-UTR region and are expressed in a tissue-specific manner.
Isoform SERCA2B (identifier: P16615-1)

Also known as: ATP2A2B; Class 2-4; HK1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Ubiquitous housekeeping isoform.
Isoform SERCA2A (identifier: P16615-2)

Also known as: ATP2A2A; Class 1; HK2;

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → AILE
Note: Cardiac/slow twitch, muscle specific isoform. Has a lower affinity for calcium and a higher catalytic turnover rate.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10421042Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
PRO_0000046196

Regions

Topological domain1 – 4848Cytoplasmic By similarity
Transmembrane49 – 69211 By similarity
Topological domain70 – 8920Lumenal By similarity
Transmembrane90 – 110212 By similarity
Topological domain111 – 253143Cytoplasmic By similarity
Transmembrane254 – 273203 By similarity
Topological domain274 – 29522Lumenal By similarity
Transmembrane296 – 313184 By similarity
Topological domain314 – 756443Cytoplasmic By similarity
Transmembrane757 – 776205 By similarity
Topological domain777 – 78610Lumenal By similarity
Transmembrane787 – 807216 By similarity
Topological domain808 – 82720Cytoplasmic By similarity
Transmembrane828 – 850237 By similarity
Topological domain851 – 89646Lumenal By similarity
Transmembrane897 – 916208 By similarity
Topological domain917 – 92913Cytoplasmic By similarity
Transmembrane930 – 948199 By similarity
Topological domain949 – 96315Lumenal By similarity
Transmembrane964 – 9842110 By similarity
Topological domain985 – 104258Cytoplasmic By similarity
Region370 – 40031Interacts with phospholamban 1 By similarity
Region575 – 59420Interacts with HAX1
Region787 – 80721Interacts with phospholamban 2 By similarity

Sites

Active site35114-aspartylphosphate intermediate By similarity
Metal binding3041Calcium 2; via carbonyl oxygen By similarity
Metal binding3051Calcium 2; via carbonyl oxygen By similarity
Metal binding3071Calcium 2; via carbonyl oxygen By similarity
Metal binding3091Calcium 2 By similarity
Metal binding7021Magnesium By similarity
Metal binding7061Magnesium By similarity
Metal binding7671Calcium 1 By similarity
Metal binding7701Calcium 1 By similarity
Metal binding7951Calcium 2 By similarity
Metal binding7981Calcium 1 By similarity
Metal binding7991Calcium 1 By similarity
Metal binding7991Calcium 2 By similarity
Metal binding9071Calcium 1 By similarity

Amino acid modifications

Modified residue2941Nitrated tyrosine Ref.5
Modified residue2951Nitrated tyrosine Ref.5
Modified residue4641N6-acetyllysine Ref.12
Modified residue5371Phosphothreonine By similarity
Modified residue6631Phosphoserine Ref.4 Ref.6 Ref.7 Ref.8 Ref.11
Cross-link143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence994 – 104249GKECV…DMFWS → AILE in isoform SERCA2A.
VSP_000358
Natural variant231G → E in DD. dbSNP rs28929478. Ref.16
VAR_008608
Natural variant391N → T in DD. Ref.15
VAR_008609
Natural variant471K → KMFLTGK in DD.
VAR_008610
Natural variant651L → S in DD; severe form.
VAR_008611
Natural variant1311R → Q in DD.
VAR_008612
Natural variant1601P → L in DD.
VAR_008613
Natural variant1861S → P in DD.
VAR_008614
Natural variant2111G → D in DD; severe form.
VAR_008615
Natural variant2231V → M in DD.
VAR_008616
Natural variant2681C → F in DD; haemorrhagic lesions.
VAR_008617
Natural variant3101G → V in DD.
VAR_008618
Natural variant3181C → R in DD; severe form.
VAR_008619
Natural variant3481I → T in DD.
VAR_008620
Natural variant3571T → K in DD. Ref.16
VAR_009508
Natural variant4121E → G in DD.
VAR_008621
Natural variant4951S → F in DD. Ref.16
VAR_008622
Natural variant5601C → R in DD; neuropsychiatric phenotype. Ref.15
VAR_008623
Natural variant6021P → L in AKV; loss of activity. Ref.17
VAR_017532
Natural variant6751F → S in DD; multiple neuropsychiatric features.
VAR_008624
Natural variant6831K → E in DD; depression.
VAR_008625
Natural variant7021D → N in DD; moderate form.
VAR_008626
Natural variant7451A → D in DD; moderate form.
VAR_008627
Natural variant7491G → R in DD. Ref.16
VAR_009509
Natural variant7541Missing in DD.
VAR_008628
Natural variant7651S → L in DD. Ref.15
VAR_008629
Natural variant7671N → S in DD; haemorrhagic lesions and neuropsychiatric phenotype.
VAR_008630
Natural variant7691G → R in DD.
VAR_008631
Natural variant8031A → T in DD; mild/moderate form.
VAR_008632
Natural variant8381A → P in DD; severe form; petit mal epilepsy.
VAR_008633
Natural variant8431V → F in DD; depression.
VAR_008634
Natural variant8751C → G in DD; retinitis pigmentosa.
VAR_008635
Natural variant9201S → Y in DD; mild/moderate/severe form; one patient with epilepsy.
VAR_008636
Natural variant9431H → R in DD; learning difficulties.
VAR_008637
Natural variant9751P → R in DD.
VAR_008638

Sequences

Sequence LengthMass (Da)Tools
Isoform SERCA2B (ATP2A2B) (Class 2-4) (HK1) [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 5462FF2DA7FB630A

FASTA1,042114,757
        10         20         30         40         50         60 
MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL 

        70         80         90        100        110        120 
LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK 

       130        140        150        160        170        180 
EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL 

       190        200        210        220        230        240 
TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV 

       250        260        270        280        290        300 
ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV 

       310        320        330        340        350        360 
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ 

       370        380        390        400        410        420 
MSVCRMFILD RVEGDTCSLN EFTITGSTYA PIGEVHKDDK PVNCHQYDGL VELATICALC 

       430        440        450        460        470        480 
NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK 

       490        500        510        520        530        540 
KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTSGV 

       550        560        570        580        590        600 
KQKIMSVIRE WGSGSDTLRC LALATHDNPL RREEMHLEDS ANFIKYETNL TFVGCVGMLD 

       610        620        630        640        650        660 
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK AFTGREFDEL 

       670        680        690        700        710        720 
NPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKAEIGIAMG 

       730        740        750        760        770        780 
SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL 

       790        800        810        820        830        840 
GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG 

       850        860        870        880        890        900 
CYVGAATVGA AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFEGVDCAIF ESPYPMTMAL 

       910        920        930        940        950        960 
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP 

       970        980        990       1000       1010       1020 
LNVTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP ATKSCSFSAC TDGISWPFVL 

      1030       1040 
LIMPLVIWVY STDTNFSDMF WS 

« Hide

Isoform SERCA2A (ATP2A2A) (Class 1) (HK2).

Checksum: DD57D12A2B24FEC1
Show »

FASTA997109,691

References

« Hide 'large scale' references
[1]"Molecular cloning of cDNAs from human kidney coding for two alternatively spliced products of the cardiac Ca2+-ATPase gene."
Lytton J., Maclennan D.H.
J. Biol. Chem. 263:15024-15031(1988) [PubMed: 2844796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS SERCA2A AND SERCA2B).
Tissue: Kidney.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SERCA2B).
Tissue: Eye.
[3]"TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesis."
Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.
Mol. Cell. Biol. 24:1758-1768(2004) [PubMed: 14749390] [Abstract]
Cited for: INTERACTION WITH TRAM2.
[4]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, MASS SPECTROMETRY.
Tissue: Epithelium.
[5]"Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging."
Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H., Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.
Am. J. Physiol. 290:H2220-H2227(2006) [PubMed: 16399855] [Abstract]
Cited for: NITRATION AT TYR-294 AND TYR-295.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, MASS SPECTROMETRY.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, MASS SPECTROMETRY.
[9]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]"The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates its protein levels to promote cell survival."
Vafiadaki E., Arvanitis D.A., Pagakis S.N., Papalouka V., Sanoudou D., Kontrogianni-Konstantopoulos A., Kranias E.G.
Mol. Biol. Cell 20:306-318(2009) [PubMed: 18971376] [Abstract]
Cited for: INTERACTION WITH HAX1.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, MASS SPECTROMETRY.
Tissue: T-cell.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-464, MASS SPECTROMETRY.
[13]"Spectrum of novel ATP2A2 mutations in patients with Darier's disease."
Sakuntabhai A., Burge S., Monk S., Hovnanian A.
Hum. Mol. Genet. 8:1611-1619(1999) [PubMed: 10441323] [Abstract]
Cited for: VARIANTS DD.
[14]"ATP2A2 mutations in Darier's disease: variant cutaneous phenotypes are associated with missense mutations, but neuropsychiatric features are independent of mutation class."
Ruiz-Perez V.L., Carter S.A., Healy E., Todd C., Rees J.L., Steijlen P.M., Carmichael A.J., Lewis H.M., Hohl D., Itin P., Vahlquist A., Gobello T., Mazzanti C., Reggazini R., Nagy G., Munro C.S., Strachan T.
Hum. Mol. Genet. 8:1621-1630(1999) [PubMed: 10441324] [Abstract]
Cited for: VARIANTS DD, TISSUE SPECIFICITY.
[15]"ATP2A2 mutations in Darier's disease and their relationship to neuropsychiatric phenotypes."
Jacobsen N.J.O., Lyons I., Hoogendoorn B., Burge S., Kwok P.-Y., O'Donovan M.C., Craddock N., Owen M.J.
Hum. Mol. Genet. 8:1631-1636(1999) [PubMed: 10441325] [Abstract]
Cited for: VARIANTS DD THR-39; ARG-560 AND LEU-765.
[16]"Mutations in ATP2A2, encoding a Ca2+ pump, cause Darier disease."
Sakuntabhai A., Ruiz-Perez V., Carter S., Jacobsen N., Burge S., Monk S., Smith M., Munro C.S., O'Donovan M.C., Craddock N., Kucherlapati R., Rees J.L., Owen M.J., Lathrop G.M., Monaco A.P., Strachan T., Hovnanian A.
Nat. Genet. 21:271-277(1999) [PubMed: 10080178] [Abstract]
Cited for: VARIANTS DD GLU-23; LYS-357; PHE-495 AND ARG-749.
[17]"Acrokeratosis verruciformis of Hopf is caused by mutation in ATP2A2: evidence that it is allelic to Darier's disease."
Dhitavat J., Macfarlane S., Dode L., Leslie N., Sakuntabhai A., MacSween R., Saihan E., Hovnanian A.
J. Invest. Dermatol. 120:229-232(2003) [PubMed: 12542527] [Abstract]
Cited for: VARIANT AKV LEU-602.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23114 mRNA. Translation: AAA53193.1.
M23116 Genomic DNA. Translation: AAA52757.1.
M23115 mRNA. Translation: AAA53194.1.
M23278, M23116 Genomic DNA. Translation: AAA52758.1.
BC035588 mRNA. Translation: AAH35588.1.
IPIIPI00177817.
IPI00219078.
PIRA31981.
B31981.
RefSeqNP_001129237.1.
NP_001672.1.
NP_733765.1.
UniGeneHs.506759

3D structure databases

SMRP16615. Positions 1-992.
ModBaseSearch...

Protein-protein interaction databases

IntActP16615. 9 interactions.
STRINGP16615.

Protein family/group databases

TCDB3.A.3.2.7. P-type ATPase (P-ATPase) superfamily.

PTM databases

PhosphoSiteP16615.

2-D gel databases

HSC-2DPAGEP16614.

Proteomic databases

PRIDEP16615.

Genome annotation databases

EnsemblENST00000313432; ENSP00000324892; ENSG00000174437; Homo sapiens. [Genome view]
GeneID488.
KEGGhsa:488.
UCSCuc001tqk.2. human.
uc001tql.2. human.

Organism-specific databases

CTD488.
GeneCardsGC12P109182.
H-InvDBHIX0010989.
HGNCHGNC:812. ATP2A2.
MIM101900. phenotype.
108740. gene.
124200. phenotype.
Orphanet79151. Acrokeratosis verruciformis of Hopf.
218. Darier disease.
PharmGKBPA71.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08565.
HOGENOMHBG456486.
HOVERGENP16615.
InParanoidP16615.
OMAPNKPSRT.
PhylomeDBP16615.

Enzyme and pathway databases

BRENDA3.6.3.8. 247.

Gene expression databases

ArrayExpressP16615.
BgeeP16615.
CleanExHS_ATP2A2.
GenevestigatorP16615.
GermOnlineENSG00000174437. Homo sapiens.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR005782. ATPase_P-typ_Ca-transp.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR000695. ATPase_P-typ_H-transp.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
[Graphical view]
PANTHERPTHR11939. ATPase_P. 1 hit.
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 4 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio2031.
SOURCESearch...

Entry information

Entry nameAT2A2_HUMAN
AccessionPrimary (citable) accession number: P16615
Secondary accession number(s): P16614
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: February 9, 2010
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents